ID A0A1F7T9G1_9BACT Unreviewed; 1521 AA.
AC A0A1F7T9G1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OGL62641.1};
GN ORFNames=A3J27_13495 {ECO:0000313|EMBL:OGL62641.1};
OS Candidatus Tectomicrobia bacterium RIFCSPLOWO2_12_FULL_69_37.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia.
OX NCBI_TaxID=1802343 {ECO:0000313|EMBL:OGL62641.1, ECO:0000313|Proteomes:UP000176745};
RN [1] {ECO:0000313|EMBL:OGL62641.1, ECO:0000313|Proteomes:UP000176745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGL62641.1}.
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DR EMBL; MGDP01000151; OGL62641.1; -; Genomic_DNA.
DR Proteomes; UP000176745; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 23..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1521 AA; 167292 MW; 01B6FC482C5CB6A0 CRC64;
MTRPHTPPPA QGLYDPAQEH DACGVCFVVD IKGRKSRRII DMAITGLEHL SHRGACGCEE
NTGDGAGILM QMPDKFLRKA CEAEGIALPE PGRYGAGIVF LPPDPIQANH CETQFEAIIR
AEGCEPLGWR EMPSDLSPVG PTARAGAPRF RQLFIGGFDP KAGRMDVERK LYVIRKQVEH
AIAKSDLTER LYFHIPSLSA QTIVYKGMLT SHQLAEVFPE LRDPDMETAL ALVHSRFSTN
TFPSWPRAHP YRYLCHNGEI NTLRGNINWM HAREALCRSE HFPELEKLLP IVVETGSDSA
MFDNVLEFLY MGGYELPHAM LMMIPEPWSG HESMDEERKA FYEYHGCIME PWDGPASIAF
TDGTTIGAVL DRNGLRPSRY YVTKDGLVVM ASEVGVLDIL PENVLLKERL HPGRIFLVDT
AEGRIIDDEE IKRRYASAKP YKKWLDGNLV PLEKLPDAPE LPEPDHETVL QRQMAFGYTE
EDLRFFLAPM ALKGDDPVGS MGTDTALPVL SNRSRLLYDY FKQLFAQVTN PPLDCIREEL
VTQMSVTIGA GGNLLNPDEA SCRQIKLESP ILDNEGLAKI GHVKHPFFKA ARLPILFPAK
EEQKGLQKAL DDLFAQADRA IAGGHNIIVI SDRGVNETMA PVPALLATAG LHHHLVRSGT
RTRVGLVLET GQARQVHQMC VLIGYGANAI NPYLAFETLD DMIRGSILTG LDHKAAVKNY
IKALKKGILK VISKMGISTI QSYCGAQVFE AVGLNKEFVD RYFTWTASRV GGIGLDVVTE
ETLIRHRRAF PERPAGKPAL DVGGEIQWRR DGEIHLFNPE TVFKLQHATR TGQFGVFREY
TKRVDDQSRG LATLRGLFEF KPARKPVPLE EVEPVESVVK RFATGAMSYG SISQEAHETL
AIAMNRLGGK SNTGEGGEDP ARYVPDANGD SRRSAIKQVA SGRFGVTSEY LVNADDLQIK
MAQGAKPGEG GQLPGHKVYP WIAKVRYSTP GVGLISPPPH HDIYSIEDLA QLIYDLKNGN
PRARIHVKLV SEVGVGTVAA GVAKAHSDVV LISGHDGGTG ASPITSIKHA GTPWELGLAE
TQQVLVLNKL RDRIVVQVDG QLKTGRDVVI AALLGADEFG FATAPLVVMG CVMMRVCHLN
TCPVGIATQD PELRKKFTGK PEFVENFFRF IAQEVREYMS LLGFRTMAEM IGRVDRINVR
KALDHWKAKG LDYAAILHKP DMGPGVAIRC VRGQDHGLEK TLDMTTLLPA CREAVEKKAP
VTLRLRIENV NRTVGTILGS EISRRHGAEG LPEDTVSIHF KGSAGQSFGA FIPKGVTLIL
EGDSNDYMGK GLSGGKIVVF PPRESSFTAE RNILIGNVAL YGATGGEAYF RGIAGERFCV
RNSGAHTVVE GVGDHGCEYM TGGRVVVLGR SGRNFAAGMS GGIAYVLDEA GDFRRRCNME
MVDLEELVVP DDVEEAKTLI RSHANYTGSE VAQRVLARWA ECQPKFVKIM PRDYKRALTA
IQRAKEQGIP WEVAVMEGAH G
//
